CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012413
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar and coiled-body phosphoprotein 1 
Protein Synonyms/Alias
 140 kDa nucleolar phosphoprotein; Nopp140; Hepatitis C virus NS5A-transactivated protein 13; HCV NS5A-transactivated protein 13; Nucleolar 130 kDa protein; Nucleolar phosphoprotein p130 
Gene Name
 NOLC1 
Gene Synonyms/Alias
 KIAA0035; NS5ATP13 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33QLSEVANKFAKATGAacetylation[1, 2, 3, 4, 5]
33QLSEVANKFAKATGAubiquitination[5, 6]
36EVANKFAKATGATQQacetylation[2]
76QANGPVAKKAKKKASacetylation[5]
80PVAKKAKKKASSSDSmethylation[7]
193KITPVTVKAQTKAPPubiquitination[5]
197VTVKAQTKAPPKPARubiquitination[5]
390TTKNSSNKPAVTTKSacetylation[5]
401TTKSPAVKPAAAPKQacetylation[5]
415QPVGGGQKLLTRKADacetylation[1, 4, 5, 8]
446KKMVATTKPKATAKAacetylation[5]
505AGGAAPSKPASAKKGacetylation[5]
510PSKPASAKKGKAESSacetylation[5]
601EAETPQAKKIKLQTPacetylation[5]
647ADNSFDAKRGAAGDWacetylation[5]
647ADNSFDAKRGAAGDWubiquitination[9, 10]
663ERANQVLKFTKGKSFacetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [10] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Related to nucleologenesis, may play a role in the maintenance of the fundamental structure of the fibrillar center and dense fibrillar component in the nucleolus. It has intrinsic GTPase and ATPase activities. May play an important role in transcription catalyzed by RNA polymerase I. 
Sequence Annotation
 DOMAIN 10 42 LisH.
 REPEAT 84 95 Acidic serine cluster 1.
 REPEAT 125 136 Acidic serine cluster 2.
 REPEAT 167 178 Acidic serine cluster 3.
 REPEAT 221 232 Acidic serine cluster 4.
 REPEAT 264 275 Acidic serine cluster 5.
 REPEAT 325 336 Acidic serine cluster 6.
 REPEAT 363 375 Acidic serine cluster 7.
 REPEAT 425 436 Acidic serine cluster 8.
 REPEAT 470 481 Acidic serine cluster 9.
 REPEAT 519 529 Acidic serine cluster 10.
 REPEAT 555 566 Acidic serine cluster 11.
 REGION 84 566 11 X 12 AA approximate repeats of an
 REGION 204 382 Interacts with RPA194.
 MOTIF 68 82 Nuclear localization signal (Potential).
 MOTIF 384 587 Nuclear localization signal (Potential).
 MOTIF 601 617 Nuclear localization signal (Potential).
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 87 87 Phosphoserine.
 MOD_RES 90 90 Phosphoserine.
 MOD_RES 91 91 Phosphoserine.
 MOD_RES 366 366 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 415 415 N6-acetyllysine.
 MOD_RES 508 508 Phosphoserine.
 MOD_RES 538 538 Phosphoserine.
 MOD_RES 563 563 Phosphoserine.
 MOD_RES 580 580 Phosphoserine.
 MOD_RES 582 582 Phosphoserine.
 MOD_RES 607 607 Phosphothreonine.
 MOD_RES 610 610 Phosphothreonine.
 MOD_RES 622 622 Phosphoserine.
 MOD_RES 643 643 Phosphoserine.
 MOD_RES 663 663 N6-acetyllysine.
 MOD_RES 686 686 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 699 AA 
Protein Sequence
MADAGIRRVV PSDLYPLVLG FLRDNQLSEV ANKFAKATGA TQQDANASSL LDIYSFWLKS 60
AKVPERKLQA NGPVAKKAKK KASSSDSEDS SEEEEEVQGP PAKKAAVPAK RVGLPPGKAA 120
AKASESSSSE ESSDDDDEED QKKQPVQKGV KPQAKAAKAP PKKAKSSDSD SDSSSEDEPP 180
KNQKPKITPV TVKAQTKAPP KPARAAPKIA NGKAASSSSS SSSSSSSDDS EEEKAAATPK 240
KTVPKKQVVA KAPVKAATTP TRKSSSSEDS SSDEEEEQKK PMKNKPGPYS SVPPPSAPPP 300
KKSLGTQPPK KAVEKQQPVE SSEDSSDESD SSSEEEKKPP TKAVVSKATT KPPPAKKAAE 360
SSSDSSDSDS SEDDEAPSKP AGTTKNSSNK PAVTTKSPAV KPAAAPKQPV GGGQKLLTRK 420
ADSSSSEEES SSSEEEKTKK MVATTKPKAT AKAALSLPAK QAPQGSRDSS SDSDSSSSEE 480
EEEKTSKSAV KKKPQKVAGG AAPSKPASAK KGKAESSNSS SSDDSSEEEE EKLKGKGSPR 540
PQAPKANGTS ALTAQNGKAA KNSEEEEEEK KKAAVVVSKS GSLKKRKQNE AAKEAETPQA 600
KKIKLQTPNT FPKRKKGEKR ASSPFRRVRE EEIEVDSRVA DNSFDAKRGA AGDWGERANQ 660
VLKFTKGKSF RHEKTKKKRG SYRGGSISVQ VNSIKFDSE 699 
Gene Ontology
 GO:0015030; C:Cajal body; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0007000; P:nucleolus organization; IEA:Compara.
 GO:0006364; P:rRNA processing; TAS:ProtInc. 
Interpro
 IPR006594; LisH_dimerisation.
 IPR007718; SRP40_C. 
Pfam
 PF05022; SRP40_C 
SMART
 SM00667; LisH 
PROSITE
 PS50896; LISH 
PRINTS